2ZWU

Substrate binding induces structural changes in cytochrome P450cam

(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 80-83

• PubMed: 19193991 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309108044114
• Primary Citation of Related Structures:  
  2ZWT, 2ZWU


• PubMed Abstract: 
  

  The binding of (+)-camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron-transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)-camphor were determined by X-ray crystallography at 1.30-1.35 A resolution, revealing the structures of the substrate-free and substrate-bound forms. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to the redox-potential change.

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Organizational Affiliation: 

Institute for Protein Research, Osaka University, Suita 565-0871, Japan.